3.5.99.10: 2-iminobutanoate/2-iminopropanoate deaminase
This is an abbreviated version!
For detailed information about 2-iminobutanoate/2-iminopropanoate deaminase, go to the full flat file.
Word Map on EC 3.5.99.10
-
3.5.99.10
-
enterica
-
2-aminoacrylate
-
pyridoxal
-
plp-dependent
-
deaminases
-
dehydratase
-
5'-phosphate
-
phosphoribosylamine
-
lessons
-
perchloric
-
d-amino
-
anthranilate
-
branched-chain
-
renamed
-
untargeted
-
5'-phosphate-dependent
-
unchecked
-
acid-soluble
-
thiamine
-
archetypal
- 3.5.99.10
- enterica
- 2-aminoacrylate
- pyridoxal
-
plp-dependent
- deaminases
- dehydratase
- 5'-phosphate
-
phosphoribosylamine
-
lessons
-
perchloric
-
d-amino
- anthranilate
-
branched-chain
-
renamed
-
untargeted
-
5'-phosphate-dependent
-
unchecked
-
acid-soluble
- thiamine
-
archetypal
Reaction
Synonyms
ACIAD3089, AtRidA, enamine/imine deaminase, endoribonuclease L-PSP family protein, imine deaminase, PA0814, PA5083, PFL_1385, PSPTO_0102, PSPTO_3006, reactive intermediate deaminase, reactive intermediate deaminase A, Rid1, Rid2, Rid3, ridA, ST0811, yjgF, YjgF_endoribonc domain-containing protein
ECTree
3.5.99.10 2-iminobutanoate/2-iminopropanoate deaminaseAdvanced search results
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results (Substrates Products
Substrates Products on EC 3.5.99.10 - 2-iminobutanoate/2-iminopropanoate deaminase
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SUBSTRATE 
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
2-aminocrotonate + H2O
2-oxobutanoate + NH3
-
-
-
?
2-aminoacrylate + H2O
pyruvate + NH3
-
-
-
?
2-aminoacrylate + H2O
pyruvate + NH3
-
-
-
?
2-aminoacrylate + H2O
pyruvate + NH3
-
-
-
?
2-iminobutanoate + H2O
2-oxobutanoate + NH3
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
-
-
?
2-iminobutanoate + H2O
2-oxobutanoate + NH3
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
-
-
?
2-iminobutanoate + H2O
2-oxobutanoate + NH3
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
-
-
?
2-iminobutanoate + H2O
2-oxobutanoate + NH3
-
-
-
?
2-iminobutanoate + H2O
2-oxobutanoate + NH3
-
-
-
?
2-iminobutanoate + H2O
2-oxobutanoate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
the enzyme catalyses the hydrolytic deamination of imine intermediates formed by several types of pyridoxal-5'-phosphate-dependent dehydratases, such as EC 4.3.1.19, threonine ammonia-lyase and EC 4.3.1.17, L-serine ammonia-lyase. The reactions, which can occur spontaneously, are accelerated to minimize the cellular damage that could be caused by these reactive intermediates
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
2-iminopropanoate + H2O
pyruvate + NH3
-
-
-
?
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-aminoacid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
a pyruvate molecule binds to the interface between two subunits, and the recognition of pyruvate is achieved by the interactions with residues R165 and T167. The enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
-
a pyruvate molecule binds to the interface between two subunits, and the recognition of pyruvate is achieved by the interactions with residues R165 and T167. The enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA. Rid2 and Rid3 proteins deaminate iminoarginine produced by DauA
-
-
-
additional information
?
-
addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA)
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
proposed mechanism of RidA-dependent enamine and imine catalysis, overview. Consistent with RidA enzymes acting on iminium ion substrates, when iminium ions are generated directly via FAD-dependent oxidases, inclusion of RidA increases the rate of hydrolysis in vitro. But it remains unclear whether RidA decreases enamine accumulation by binding the enamine and facilitating both iminium ion formation and subsequent hydrolysis or whether RidA decreases enamine levels simply through increased consumption of its iminium ion tautomer
-
-
-
additional information
?
-
the enzyme reduces semicarbazone formation
-
-
-
additional information
?
-
enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
-
-
-
additional information
?
-
addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA)
-
-
-
additional information
?
-
proposed mechanism of RidA-dependent enamine and imine catalysis, overview. Consistent with RidA enzymes acting on iminium ion substrates, when iminium ions are generated directly via FAD-dependent oxidases, inclusion of RidA increases the rate of hydrolysis in vitro. But it remains unclear whether RidA decreases enamine accumulation by binding the enamine and facilitating both iminium ion formation and subsequent hydrolysis or whether RidA decreases enamine levels simply through increased consumption of its iminium ion tautomer
-
-
-
additional information
?
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the enzyme reduces semicarbazone formation
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additional information
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enzyme assay is coupled using Crotalus adamanteus L-amino acid oxidase, bovine liver catalase, and the Rid enzyme. When arginine is used as a LOX substrate, representatives from the Rid1, Rid2 and Rid3 subfamilies appear to have more deaminase activity than RidA
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additional information
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addition of purified RidA to the Salmonella enterica IlvA reactions increases the rate of ketoacid formation, showing that RidA catalyzes the hydrolysis of enamines derived from threonine (2-aminocrotonate, 2AC) and serine (2-aminoacrylate, 2AA)
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additional information
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proposed mechanism of RidA-dependent enamine and imine catalysis, overview. Consistent with RidA enzymes acting on iminium ion substrates, when iminium ions are generated directly via FAD-dependent oxidases, inclusion of RidA increases the rate of hydrolysis in vitro. But it remains unclear whether RidA decreases enamine accumulation by binding the enamine and facilitating both iminium ion formation and subsequent hydrolysis or whether RidA decreases enamine levels simply through increased consumption of its iminium ion tautomer
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